| IED ID | IndEnz0002004978 |
| Enzyme Type ID | protease004978 |
| Protein Name |
Separin EC 3.4.22.49 Separase |
| Gene Name | ESP1 YGR098C |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MMVKQEEPLNEISPNTPMTSKSYLLNDTLSKVHHSGQTRPLTSVLSGDASSNSIGILAMHNNIIRDFTKIASNNIDLAIEDITTVDHSLNSIYSLLKSHHMWGHINSTVKQHLMIIVKLINNNALGLASSEIIFLFNETNLFQAHSLKNILLADFSTWNDYYLSNLKILALQIILKRKLVDEYLPHILELFSHDKRYLLKDPNLKAHALTKIVLSFFSVTTSCKVLFGLKFLQYIKQFKLPFKKFISNITVECFSKNLLHKNYLEMGPNKIYLNSFYLSYSMLYDGLDKIMLLDILSYEETTEVQRAIKSKKEFNEYCNMSENRLLWSCISVDDLNVILENATNFLQNKGKHISATLKCLVCLWSTIRLEGLPKNKDILRQFDCTVIYINSNIKSINDESAAALLSELLGVLSEICIDYKEPKRLSNIISVLFNASVLFKSHSFLLKTANLEISNVLISNDSKTSHRTILKFEKFISSAQSAQKKIEIFSCLFNVYCMLRNDTLSFVFDFCQNAFIHCFTRLKITKFIEFSNSSEIMLSVLYGNSSIENIPSENWSQLSRMIFCSLRGIFDLDPLELNNTFDKLHLLNKYELLIRIVYLLNLDMSKHLTTNLSKITKLYINKWLQKSDEKAERISSFEMDFVKMLLCYLNFNNFDKLSIELSLCIKSKEKYYSSIVPYADNYLLEAYLSLYMIDDALMMKNQLQKTMNLSTAKIEQALLHASSLINVHLWDSDLTAFQIYFGKTLPAMKPELFDINNDHNLPMSLYIKVILLNIKIFNESAKLNIKAGNVISAVIDCRKAQNLALSLLKKKNKLSQGSRLALLKSLSFSFFQLIKIHIRIGSARDCEFYSKELSRIISDLEEPIIVYRCLHFLHRYYMITEQTCLQNITLGKANKAFDYLDAEADITSLTMFLYDNKEFVKLEQSLVLYFGDQLEKTFLPNLWKLHLGKDIDDSICLSEYMPKNVINRVHNMWQKVMSQLEEDPFFKGMFESTLGIPSSLPVIPSTMPNNILKTPSKHSTGLKLCDSPRSSSMTPRGKNIRQKFDRIAAISKLKQMKELLESLKLDTLDNHELSKISSLSSLTLTILSNITSIHNAESSLITNFSLTDLPRHMPLLFDKVLNNIDNKNYREFRVSSLIAPNNISTITESIRVSAAQKDLMESNLNINVITIDFCPITGNLLLSKLEPRRKRRTHLRLPLIRSNSRDLDEVHLSFPEATKKLLSIINESNQTTSVEVTNKIKTREERKSWWTTRYDLDKRMQQLLNNIENSWFNGVQGFFSPEVVDNSLFEKFKDKFYEILHQNLPSRKLYGNPAMFIKVEDWVIELFLKLNPQEIDFLSKMEDLIYFVLDILLFHGEENAYDEIDFSMLHVQLEEQIKKYRATMTTNSIFHTFLVVSSSCHLFPWECLSFLKDLSITRVPSYVCLNKLLSRFHYQLPLQVTIEDNISMILNPNGDLSRTESKFKGMFQKIIDAKPSSQLVMNEKPEEETLLKMLQNSNLFVYIGHGGGEQYVRSKEIKKCTKIAPSFLLGCSSAAMKYYGKLEPTGTIYTYLLGGCPMVLGNLWDVTDKDIDKFSEELFEKMGFRCNTDDLNGNSLSVSYAVSKSRGVCHLRYLNGAAPVIYGLPIKFVS |
| Enzyme Length | 1630 |
| Uniprot Accession Number | Q03018 |
| Absorption | |
| Active Site | ACT_SITE 1531; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: It is inactivated via its interaction with PDS1, which probably covers its active site. PDS1 degradation at anaphase, liberates it and triggers MCD1 cleavage. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=All bonds known to be hydrolyzed by this endopeptidase have arginine in P1 and an acidic residue in P4. P6 is often occupied by an acidic residue or by a hydroxy-amino-acid residue, the phosphorylation of which enhances cleavage.; EC=3.4.22.49; |
| DNA Binding | |
| EC Number | 3.4.22.49 |
| Enzyme Function | FUNCTION: Caspase-like protease, which plays a central role in the chromosome segregation by cleaving the MCD1/SCC1 subunit of the cohesin complex at the onset of anaphase. During most of the cell cycle, it is inactivated by securin/PDS1 protein. It also promotes anaphase spindle elongation. A component of the FEAR (CDC14 early anaphase release) network which promotes CDC14 release from the nucleolus during early anaphase. Cleaves SLK19. {ECO:0000269|PubMed:10403247, ECO:0000269|PubMed:11149918, ECO:0000269|PubMed:11832211, ECO:0000269|PubMed:9635435}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (22); Chain (1); Domain (1); Helix (91); Mutagenesis (1); Region (1); Sequence conflict (10); Turn (14) |
| Keywords | 3D-structure;Calcium;Chromosome partition;Cytoplasm;Cytoskeleton;Hydrolase;Nucleus;Protease;Reference proteome;Thiol protease |
| Interact With | Q00362; P40316 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11149918}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:11149918}. Cytoplasm {ECO:0000269|PubMed:11149918}. Note=Accumulates in the nucleus in G2 and is mobilized onto the spindle pole bodies and spindle midzone at anaphase onset, where it persists into midanaphase. The association with MCD1 may be important for its nuclear targeting. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 5U1S; 5U1T; |
| Mapped Pubmed ID | 10322145; 10403242; 10444592; 10519004; 10651900; 10679389; 10740270; 11081625; 11146641; 11163155; 11163156; 11309624; 11511341; 11533655; 11698195; 11702777; 11754482; 11805826; 11832245; 11864593; 11985612; 12050115; 12101125; 12142526; 12498686; 12598903; 12600308; 12646872; 12724769; 12769836; 14551257; 14585836; 15130497; 15190202; 15241476; 15521820; 15655374; 15703941; 15887295; 16126387; 16429126; 16554755; 16713564; 16839182; 16946739; 17050679; 17562791; 17573771; 18235228; 18321989; 18368920; 18430955; 18680435; 18719252; 18762578; 18927509; 19144818; 19268588; 19270692; 19299562; 19308704; 19416362; 19536198; 19841731; 19887903; 20230747; 20407133; 20421994; 21518961; 21750572; 21936842; 22046265; 22121979; 22188402; 22383977; 22481439; 22510435; 22572959; 22677545; 22814605; 22842922; 23133392; 23169651; 23212898; 23831059; 24013422; 24205865; 24223874; 24395824; 25822502; 25823586; 26272996; 27048816; 27210759; 27418100; 27450768; 28017619; 28146474; 29561844; 30219856; 3072479; 32402080; 8836740; 9914173; 9920414; |
| Motif | |
| Gene Encoded By | |
| Mass | 187,447 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.49; |